PDBsum entry 3dp5

Electron transport

PDB id: 3dp5

Contents

Protein chain

99 a.a. *

Ligands

SO4

HEC

Waters ×117

* Residue conservation analysis

PDB id:

3dp5

Name:

Electron transport

Title:

Crystal structure of geobacter sulfurreducens omcf with n-terminal strep-tag ii

Structure:

CytochromE C family protein. Chain: a. Fragment: unp residues 26-104, omcf. Synonym: omcf. Engineered: yes

Source:

Geobacter sulfurreducens. Organism_taxid: 35554. Strain: pca. Gene: gsu2432. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.86Å R-factor: 0.172 R-free: 0.210

Authors:

P.Lukat,M.Hoffmann,O.Einsle

Key ref:

P.Lukat et al. (2008). Crystal packing of the c(6)-type cytochrome OmcF from Geobacter sulfurreducens is mediated by an N-terminal Strep-tag II. Acta Crystallogr D Biol Crystallogr, 64, 919-926. PubMed id: 18703839 DOI: 10.1107/S0907444908021306

Date:

07-Jul-08 Release date: 02-Sep-08

Protein chain

Q74AE4  (Q74AE4_GEOSL) -  Lipoprotein cytochrome c, 1 heme-binding site from Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)

Seq: 104 a.a.

Struc: 99 a.a.*

* PDB and UniProt seqs differ at 20 residue positions (black crosses)

DOI no: 10.1107/S0907444908021306

Acta Crystallogr D Biol Crystallogr 64:919-926 (2008)

PubMed id: 18703839

Crystal packing of the c(6)-type cytochrome OmcF from Geobacter sulfurreducens is mediated by an N-terminal Strep-tag II.

P.Lukat, M.Hoffmann, O.Einsle.

ABSTRACT

The putative outer membrane c-type cytochrome OmcF from Geobacter sulfurreducens contains a single haem group and shows homology to soluble cytochromes c(6), a class of electron-transfer proteins that are typically found in cyanobacterial photosynthetic electron-transfer chains. OmcF was overexpressed heterologously in Escherichia coli as an N-terminal Strep-tag II fusion protein and isolated using streptactin-affinity chromatography followed by size-exclusion chromatography. The structure was solved by Fe SAD using data collected to a resolution of 1.86 A on a rotating copper-anode X-ray generator. In the crystal, packing interactions in one dimension were exclusively mediated through the Strep-tag II sequence. The tag and linker regions were in contact with three further monomers of OmcF, leading to a well defined electron-density map for this engineered and secondary-structure-free region of the molecule.

Selected figure(s)

Figure 4.
Figure 4 Stereo representation of the cytochrome c[6] domain of G. sulfurreducens OmcF. The single haem group of OmcF is covalently linked to the peptide chain via a bonding motif with sequence CAGCH (residues 35-39). His39 functions as a proximal axial ligand to the haem Fe atom, while the distal axial ligand is Met79. Every tenth residue in the sequence is marked.

Figure 7.
Figure 7 Stereo representation showing the interactions of the linker (blue) and Strep-tag II region (red) with three neighbouring monomers as detailed in Table 3-. Hydrogen-bonding interactions within the linker/tag are shown in blue and interactions with other monomers in red. Five of the seven observed hydrogen-bonding interactions are formed by the Strep-tag II and the other two are formed by the linker region.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2008, 64, 919-926) copyright 2008.

Figures were selected by an automated process.